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An infrared spectroscopy approach to follow β-sheet formation in peptide amyloid assemblies

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Seo,  Jongcheol
Molecular Physics, Fritz Haber Institute, Max Planck Society;

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Hoffmann,  Waldemar
Molecular Physics, Fritz Haber Institute, Max Planck Society;
Institute of Chemistry and Biochemistry, Freie Universität Berlin;

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Warnke,  Stephan
Molecular Physics, Fritz Haber Institute, Max Planck Society;

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Huang,  Xing
Inorganic Chemistry, Fritz Haber Institute, Max Planck Society;

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Gewinner,  Sandy
Molecular Physics, Fritz Haber Institute, Max Planck Society;

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Schöllkopf,  Wieland
Molecular Physics, Fritz Haber Institute, Max Planck Society;

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Helden,  Gert von
Molecular Physics, Fritz Haber Institute, Max Planck Society;

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Pagel,  Kevin
Molecular Physics, Fritz Haber Institute, Max Planck Society;
Institute of Chemistry and Biochemistry, Freie Universität Berlin;

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Citation

Seo, J., Hoffmann, W., Warnke, S., Huang, X., Gewinner, S., Schöllkopf, W., et al. (2017). An infrared spectroscopy approach to follow β-sheet formation in peptide amyloid assemblies. Nature Chemistry, 9(1), 39-44. doi:10.1038/nchem.2615.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002C-4E9C-5
Abstract
Amyloidogenic peptides and proteins play a crucial role in a variety of neurodegenerative disorders such as Alzheimer's and Parkinson's disease. These proteins undergo a spontaneous transition from a soluble, often partially folded form, into insoluble amyloid fibrils that are rich in β-sheets. Increasing evidence suggests that highly dynamic, polydisperse folding intermediates, which occur during fibril formation, are the toxic species in the amyloid-related diseases. Traditional condensed-phase methods are of limited use for characterizing these states because they typically only provide ensemble averages rather than information about individual oligomers. Here we report the first direct secondary-structure analysis of individual amyloid intermediates using a combination of ion mobility spectrometry–mass spectrometry and gas-phase infrared spectroscopy. Our data reveal that oligomers of the fibril-forming peptide segments VEALYL and YVEALL, which consist of 4–9 peptide strands, can contain a significant amount of β-sheet. In addition, our data show that the more-extended variants of each oligomer generally exhibit increased β-sheet content.